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310 results on '"Behlke, Joachim"'

14. Molecular dissection of the interaction between amyloid precursor protein and its neuronal trafficking receptor SorLA/LR11

Author

Andersen, Olav M., Schmidt, Vanessa, Spoelgen, Robert, Gliemann, Jorgen, Behlke, Joachim, Galatis, Denise, McKinstry, William J., Parker, Michael W., Masters, Colin L., Hyman, Bradley T., Cappai, Roberto, and Willnow, Thomas E.

Subjects
Protein binding -- Research, Alzheimer's disease -- Research, Biological sciences, Chemistry
Abstract

The exact binding sites that are responsible for the interaction of the amyloid precursor protein (APP) and sorLA in neurons are delineated and their mode of action are characterized as a first approach toward elucidating this novel molecular mechanism that controls APP trafficking and processing the brain. The results help in understanding the molecular determinants of neuronal APP trafficking and processing and on possible targets for intervention with senile plaque formation in patients with Alzheimer's disease (AD).

Published
2006

15. Size determination of cyanobacterial and higher plant photosystem II by gel permeation chromatography, light scattering, and ultracentrifugation

Author

Zouni, Athina, Kern, Jan, Frank, Joachim, Hellweg, Thomas, Behlke, Joachim, Saenger, Wolfram, and Irrgang, Klaus-Dieter

Subjects
Bacteria, Thermophilic -- Research, Gel permeation chromatography -- Methods, Cyanobacteria -- Research, Biological sciences, Chemistry
Abstract

The oxygen-evolving photosystem II core complexes (PSIIcc) from the thermophilic cyanobacterium Thermosynechococcus elongatus (PSIIccTe) and the higher plant Spinacia oleracea (PSIIccSo) are isolated from the thylakoid membrane by solubilization with n-dodecyl-beta-D-maltoside, purified and characterized by gel permeation chromatography (GPC), dynamic light scattering (DLS), and analytical centrifugation (AUC). The results are discussed from a crystallization point of view.

Published
2005

20. Interaction of fluorescence labeled single-stranded DNA with hexameric DNA-helicase RepA: a photon and fluorescence correlation spectroscopy study

Author

Xu, Hai, Frank, Joachim, Trier, Ulrike, Hammer, Stefanie, Schroder, Werner, Behlke, Joachim, Schafer-Korting, Monika, Holzwarth, Josef F., and Saenger, Wolfram

Subjects
Fluorescence spectroscopy -- Methods, DNA-ligand interactions -- Analysis, DNA binding proteins -- Analysis, Structure-activity relationships (Biochemistry) -- Analysis, Biological sciences, Chemistry
Abstract

Photon and fluorescence correlation spectroscopic studies yield the same apparent hydrodynamic radii measurement for the hexameric RepA DNA-helicase dimer and its complex with the single-stranded DNA. Data reveal that the RepA DNA-helicase binds to single-stranded DNA optimally under acidic conditions leading to a structural change in the former.

Published
2001

21. Regulation of phosphotransferase activity of hexokinase 2 from Saccharomyces cerevisiae by modification of serine-14

Author

Golbik, Ralph, Naumann, Manfred, Otto, Albrecht, Muller, Eva-Christina, Behlke, Joachim, Reuter, Renate, Hubner, Gerhard, and Kriegel, Thomas M.

Subjects
Saccharomyces -- Research, Enzymes -- Structure-activity relationship, Amino acids -- Structure-activity relationships, Phosphorylation -- Physiological aspects, Biological sciences, Chemistry
Abstract

Research demonstrates that the monomeric form of hexokinase 2 of Saccharomyces cerevisiae exhibits high-affinity to its substrates mediated by substitution of serine-14 with glutamate and subsequent pseudophosphorylation of the enzyme. Data further point out that phosphorylation at serine-14 may be involved in glucose signaling.

Published
2001

22. Water-soluble beta-sheet models which self-assemble into fibrillar structures

Author

Janek, Katharina, Behlke, Joachim, Zipper, Josef, Fabian, Heinz, Georgalis, Yannis, Beyermann, Michael, Bienert, Michael, and Krause, Eberhard

Subjects
Peptides -- Synthesis, Conformational analysis -- Research, Molecular association -- Research, Biological sciences, Chemistry
Abstract

Research was conducted to examine the water-soluble de novo beta-sheet peptides which self-assemble into fibrillar structures. Conformational analyses suggest differing potentials of the various peptides to adopt the beta-sheet conformation. Both the influence of D-amino acid substitution and the length of the secondary structure domain were correlated with the beta-sheet stability and the association behavior. Results demonstrate that strong association of beta-strands leads to fibrillar structures which can bind Congo Red and exhibit birefringence.

Published
1999

25. Hexokinase 2 from Saccharomyces cerevisiae: regulation of oligomeric structure by in vivo phosphorylation at serine-14

Author

Behlke, Joachim, Heidrich, Katja, Naumann, Manfred, Miller, Eva-Christian, Otto, Albrecht, Reuter, Renate, and Kriegel, Thomas

Subjects
Saccharomyces -- Research, Phosphorylation -- Research, Protein kinases -- Research, Biological sciences, Chemistry
Abstract

Research was conducted to demonstrate that serine-14 phosphorylation in Saccharomyces cerevisiae influences the oligomeric state of hexokinase through site-directed mutagenesis and sedimentation analysis. It was also noted that its substitution by glutamate caused complete dissociation while glutamate exchange for serine-157 did not. It is concluded that the in vivo phosphorylation at serine-14 may offer a mechanism to enhance glucose utilization from low level.

Published
1998

26. Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions

Author

Behlke, Joachim, Ristau, Otto, and Schonfeld, Hans-Joachim

Subjects
Escherichia coli -- Research, Nucleotides -- Research, Centrifuges -- Research, Bacteria -- Research, Biological sciences, Chemistry
Abstract

Analytical centrifugation was performed to understand the quatenary structures and interaction in solution of the GroE chaperonin system. The heterogenous association between GroEL and GroEs oligomers under different conditions was analyzed by studying the sedimentation equilibrium in the analytical centrifuge. Low amounts of asymmetrical GroEL- GroES2 complexes were observed under in vivo conditions.

Published
1997

27. Autophosphorylation-inactivation site of hexokinase 2 in Saccharomyces cerevisiae

Author

Heidrich, Katja, Otto, Albrecht, Behlke, Joachim, Rush, John, Wenzel, Klaus-Wolfgang, and Kriegel, Thomas

Subjects
Phosphorylation -- Analysis, Enzymes -- Research, Saccharomyces -- Research, Enzymatic analysis -- Usage, Mass spectrometry -- Usage, Amino acid sequence -- Usage, Molecular genetics -- Usage, Biological sciences, Chemistry
Abstract

Enzyme assay, peptide sequencing and size determination by mass spectrometry were done to identify the site of autophosphorylative inactivation of hexokinase 2 derived from Saccharomyces cerevisiae. The results confirmed that the site is localized at serine-158. This was verified by mutation analysis wherein serine-158 was replaced by alanine and cysteine which resulted in decreased enzyme activity. Mutation of the same amino acid to glutamate, on the other hand, led to complete loss of catalytic activity. It was also found that phosphoserine/phosphothreonine-specific protein phosphatase-2A can cause complete reversion of the autophosphorylative inactivation of hexokinase 2.

Published
1997

50. Structural and functional characterization of human Iba proteins

Author

Schulze, Jörg O, Quedenau, Claudia, Roske, Yvette, Adam, Thomas, Schüler, Herwig, Behlke, Joachim, Turnbull, Andrew P, Sievert, Volker, Scheich, Christoph, Mueller, Uwe, Heinemann, Udo, Büssow, Konrad, and Max Delbrück Center for Molecular Medicine, Berlin, Germany.

Subjects
Models, Molecular, Calcium-Binding Proteins, Microfilament Proteins, Molecular Sequence Data, Crystallography, X-Ray, Actins, DNA-Binding Proteins, Hela Cells, Humans, Calcium, Amino Acid Sequence, Shigella, Dimerization, Sequence Alignment
Abstract

Iba2 is a homolog of ionized calcium-binding adapter molecule 1 (Iba1), a 17-kDa protein that binds and cross-links filamentous actin (F-actin) and localizes to membrane ruffles and phagocytic cups. Here, we present the crystal structure of human Iba2 and its homodimerization properties, F-actin cross-linking activity, cellular localization and recruitment upon bacterial invasion in comparison with Iba1. The Iba2 structure comprises two central EF-hand motifs lacking bound Ca2+. Iba2 crystallized as a homodimer stabilized by a disulfide bridge and zinc ions. Analytical ultracentrifugation revealed a different mode of dimerization under reducing conditions that was independent of Ca2+. Furthermore, no binding of Ca2+ up to 0.1 mM was detected by equilibrium dialysis. Correspondingly, Iba EF-hand motifs lack residues essential for strong Ca2+ coordination. Sedimentation experiments and microscopy detected pronounced, indistinguishable F-actin binding and cross-linking activity of Iba1 and Iba2 with induction of F-actin bundles. Fluorescent Iba fusion proteins were expressed in HeLa cells and co-localized with F-actin. Iba1 was recruited into cellular projections to a larger extent than Iba2. Additionally, we studied Iba recruitment in a Shigella invasion model that induces cytoskeletal rearrangements. Both proteins were recruited into the bacterial invasion zone and Iba1 was again concentrated slightly higher in the cellular extensions.

Published
2008

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